(Q40749083)

English

Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. Part 7: structure-activity studies of bicyclic 2-pyridone-containing peptidomimetics

scientific article published on March 2002

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scholarly article

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23 September 2017

Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. Part 7: structure-activity studies of bicyclic 2-pyridone-containing peptidomimetics (English)

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23 September 2017

Peter S Dragovich

1

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Peter S Dragovich

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23 September 2017

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Thomas J Prins

2

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23 September 2017

Ru Zhou

3

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23 September 2017

Theodore O Johnson

4

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23 September 2017

Edward L Brown

5

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23 September 2017

Fausto C Maldonado

6

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23 September 2017

Shella A Fuhrman

7

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23 September 2017

Leora S Zalman

8

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23 September 2017

Amy K Patick

9

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23 September 2017

David A Matthews

10

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23 September 2017

Xinjun Hou

11

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23 September 2017

James W Meador

12

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23 September 2017

Rose Ann Ferre

13

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23 September 2017

Stephen T Worland

14

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23 September 2017

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publication date

1 March 2002

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23 September 2017

Bioorganic & Medicinal Chemistry Letters

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23 September 2017

12

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23 September 2017

5

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23 September 2017

733-738

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23 September 2017

Treatment of the picornavirus common cold by inhibitors of viral uncoating and attachment

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Rhinovirus colds

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Viral proteinases

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Hydrolysis of a series of synthetic peptide substrates by the human rhinovirus 14 3C proteinase, cloned and expressed in Escherichia coli

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Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases

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Poliovirus-encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families

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Crystal structure of human cathepsin K complexed with a potent inhibitor

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Peptidyl vinyl sulphones: a new class of potent and selective cysteine protease inhibitors: S2P2 specificity of human cathepsin O2 in comparison with cathepsins S and L.

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Vinyl sulfones as mechanism-based cysteine protease inhibitors

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Structure-activity relationships for inhibition of papain by peptide Michael acceptors

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Vinylogous amino acid esters: a new class of inactivators for thiol proteases

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On the size of the active site in proteases. I. Papain

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Exploring the chiral space within the active site of alpha-thrombin with a constrained mimic of D-Phe-Pro-Arg--design, synthesis, inhibitory activity, and X-ray structure of an enzyme-inhibitor complex

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Secondary structure peptide mimetics: design, synthesis, and evaluation of beta-strand mimetic thrombin inhibitors

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Synthesis and structure-activity relationship of potent bicyclic lactam thrombin inhibitors

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Peptidomimetic design

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Concepts and progress in the development of peptide mimetics

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Design, synthesis, and evaluation of nonpeptidic inhibitors of human rhinovirus 3C protease

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Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 4. Incorporation of P1 lactam moieties as L-glutamine replacements

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Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes

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Structure-based design, synthesis, and biological evaluation of irreversible human rhinovirus 3C protease inhibitors. 1. Michael acceptor structure-activity studies.

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An efficient synthesis of a key intermediate for the preparation of the rhinovirus protease inhibitor AG7088 via asymmetric dianionic cyanomethylation of N-Boc-l-(+)-glutamic acid dimethyl ester

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Identifiers

10.1016/S0960-894X(02)00008-2

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 September 2017

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